The evolution of oxygen transport hemoglobins occurred on at least two independent
occasions. The earliest event led to myoglobin and red blood cell hemoglobin in animals. In …

Hemoglobins from the plants Parasponia andersonii (ParaHb) and Trema tomentosa
(TremaHb) are 93% identical in primary structure but differ in oxygen binding constants in …

The heme prosthetic group in hemoglobins is most often attached to the globin through
coordination of either one or two histidine side chains. Those proteins with one histidine …

Plants express three phylogenetic classes of hemoglobins (Hb) based on sequence
analyses. Class 1 and 2 Hbs are full‐length globins with the classical eight helix Mb‐like …

New developments have forced a re-evaluation of our understanding of the structure and
function of hemoglobins. Leghemoglobins regulate oxygen affinity through a mechanism …

Nonsymbiotic hemoglobins (nsHbs) are widespread in plants including bryophytes.
Bryophytes (such as mosses) are among the oldest land plants, thus an analysis of a …

Background: Nonsymbiotic hemoglobins (nsHbs) form a new class of plant proteins that is
distinct genetically and structurally from leghemoglobins. They are found ubiquitously in …

Genome of the model dicot flowering plant, Arabidopsis thaliana, a popular tool for
understanding molecular biology of plant physiology, encodes all three classes of plant …

All plants contain hemoglobins that fall into distinct phylogenetic classes. The subset of
plants that carry out symbiotic nitrogen fixation expresses hemoglobins that scavenge and …

All plants contain an unusual class of hemoglobins that display bis-histidyl coordination yet
are able to bind exogenous ligands such as oxygen. Structurally homologous …